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Calmodulin-1

 CALM1_HUMAN             Reviewed;         149 AA.
P0DP23; P02593; P62158; P70667; P99014; Q13942; Q53S29; Q61379; Q61380;
Q96HK3;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 1.
29-SEP-2021, entry version 40.
RecName: Full=Calmodulin-1 {ECO:0000312|HGNC:HGNC:1442};
Name=CALM1 {ECO:0000303|PubMed:7925473, ECO:0000312|HGNC:HGNC:1442};
Synonyms=CALM, CAM, CAM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6385987;
Wawrzynczak E.J., Perham R.N.;
"Isolation and nucleotide sequence of a cDNA encoding human calmodulin.";
Biochem. Int. 9:177-185(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=7925473; DOI=10.1111/j.1432-1033.1994.00071.x;
Rhyner J.A., Ottiger M., Wicki R., Greenwood T.M., Strehler E.E.;
"Structure of the human CALM1 calmodulin gene and identification of two
CALM1-related pseudogenes CALM1P1 and CALM1P2.";
Eur. J. Biochem. 225:71-82(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Lung, Lymph, Placenta, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT
LYS-116.
TISSUE=Brain;
PubMed=7093203; DOI=10.1021/bi00539a041;
Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H.,
Titani K.;
"Complete amino acid sequence of human brain calmodulin.";
Biochemistry 21:2565-2569(1982).
[7]
PROTEIN SEQUENCE OF 2-31 AND 92-107, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Osteosarcoma;
Bienvenut W.V., Bensaad K., Vousden K.H.;
Submitted (FEB-2008) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 15-31; 77-107 AND 128-149, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
INTERACTION WITH TTN.
PubMed=9804419; DOI=10.1038/27603;
Mayans O., van der Ven P.F.M., Wilm M., Mues A., Young P., Furst D.O.,
Wilmanns M., Gautel M.;
"Structural basis for activation of the titin kinase domain during
myofibrillogenesis.";
Nature 395:863-869(1998).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
"Proteomic characterization of the human centrosome by protein correlation
profiling.";
Nature 426:570-574(2003).
[11]
INTERACTION WITH SRY.
PubMed=12871148; DOI=10.2174/0929866033479004;
Kelly S., Yotis J., Macris M., Harley V.;
"Recombinant expression, purification and characterisation of the HMG
domain of human SRY.";
Protein Pept. Lett. 10:281-286(2003).
[12]
INTERACTION WITH USP6.
PubMed=16127172; DOI=10.1074/jbc.m505220200;
Shen C., Ye Y., Robertson S.E., Lau A.W., Mak D.O., Chou M.M.;
"Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific
protease TRE17/USP6.";
J. Biol. Chem. 280:35967-35973(2005).
[13]
INTERACTION WITH SRY.
PubMed=15746192; DOI=10.1210/me.2004-0334;
Sim H., Rimmer K., Kelly S., Ludbrook L.M., Clayton A.H., Harley V.R.;
"Defective calmodulin-mediated nuclear transport of the sex-determining
region of the Y chromosome (SRY) in XY sex reversal.";
Mol. Endocrinol. 19:1884-1892(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[15]
FUNCTION, INTERACTION WITH CCP110, AND SUBCELLULAR LOCATION.
PubMed=16760425; DOI=10.1091/mbc.e06-04-0371;
Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z.,
Salisbury J.L., Sanchez I., Dynlacht B.D.;
"CP110 cooperates with two calcium-binding proteins to regulate cytokinesis
and genome stability.";
Mol. Biol. Cell 17:3423-3434(2006).
[16]
INTERACTION WITH CEP97 AND CCP110.
PubMed=17719545; DOI=10.1016/j.cell.2007.06.027;
Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.;
"Cep97 and CP110 suppress a cilia assembly program.";
Cell 130:678-690(2007).
[17]
INTERACTION WITH KCNQ1.
PubMed=18165683; DOI=10.1074/jbc.m707541200;
Wiener R., Haitin Y., Shamgar L., Fernandez-Alonso M.C., Martos A.,
Chomsky-Hecht O., Rivas G., Attali B., Hirsch J.A.;
"The KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit
assembly and protein interaction.";
J. Biol. Chem. 283:5815-5830(2008).
[18]
INTERACTION WITH RYR1 AND RYR2.
PubMed=18650434; DOI=10.1074/jbc.m804432200;
Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F.,
Weber D.J.;
"S100A1 and calmodulin compete for the same binding site on ryanodine
receptor.";
J. Biol. Chem. 283:26676-26683(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND TYR-139, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22 AND LYS-95, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[23]
INTERACTION WITH CDK5RAP2.
PubMed=20466722; DOI=10.1074/jbc.m110.105965;
Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.;
"Conserved motif of CDK5RAP2 mediates its localization to centrosomes and
the Golgi complex.";
J. Biol. Chem. 285:22658-22665(2010).
[24]
INTERACTION WITH RUBELLA VIRUS PROTEASE/METHYLTRANSFERASE P150.
PubMed=20086014; DOI=10.1074/jbc.m109.097063;
Zhou Y., Tzeng W.P., Wong H.C., Ye Y., Jiang J., Chen Y., Huang Y.,
Suppiah S., Frey T.K., Yang J.J.;
"Calcium-dependent association of calmodulin with the rubella virus
nonstructural protease domain.";
J. Biol. Chem. 285:8855-8868(2010).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
INTERACTION WITH ORAI1.
PubMed=23109337; DOI=10.1074/jbc.m112.380964;
Liu Y., Zheng X., Mueller G.A., Sobhany M., DeRose E.F., Zhang Y.,
London R.E., Birnbaumer L.;
"Crystal structure of calmodulin binding domain of orai1 in complex with
Ca2+ calmodulin displays a unique binding mode.";
J. Biol. Chem. 287:43030-43041(2012).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[29]
INTERACTION WITH FCHO1.
PubMed=22484487; DOI=10.1038/ncb2473;
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
Tsang M., Traub L.M.;
"Distinct and separable activities of the endocytic clathrin-coat
components Fcho1/2 and AP-2 in developmental patterning.";
Nat. Cell Biol. 14:488-501(2012).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-102, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND THR-111, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[35]
FUNCTION, AND INTERACTION WITH PIK3C3.
PubMed=28890335; DOI=10.1016/j.molcel.2017.08.005;
Zhao Y.G., Chen Y., Miao G., Zhao H., Qu W., Li D., Wang Z., Liu N., Li L.,
Chen S., Liu P., Feng D., Zhang H.;
"The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates SERCA Activity
to Control ER-Isolation Membrane Contacts for Autophagosome Formation.";
Mol. Cell 67:974.e6-989.e6(2017).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[37]
INTERACTION WITH KIF1A.
PubMed=30021165; DOI=10.1016/j.celrep.2018.06.071;
Stucchi R., Plucinska G., Hummel J.J.A., Zahavi E.E., Guerra San Juan I.,
Klykov O., Scheltema R.A., Altelaar A.F.M., Hoogenraad C.C.;
"Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM Controls
DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to Postsynaptic Sites.";
Cell Rep. 24:685-700(2018).
[38]
INTERACTION WITH SLC9A1.
PubMed=30287853; DOI=10.1038/s41598-018-33096-5;
Fuchs S., Hansen S.C., Markones M., Mymrikov E.V., Heerklotz H., Hunte C.;
"Calcineurin B homologous protein 3 binds with high affinity to the CHP
binding domain of the human sodium/proton exchanger NHE1.";
Sci. Rep. 8:14837-14837(2018).
[39]
INTERACTION WITH KCNN3.
PubMed=31155282; DOI=10.1016/j.ajhg.2019.04.012;
Bauer C.K., Schneeberger P.E., Kortuem F., Altmueller J.,
Santos-Simarro F., Baker L., Keller-Ramey J., White S.M., Campeau P.M.,
Gripp K.W., Kutsche K.;
"Gain-of-function mutations in KCNN3 encoding the small-conductance Ca2+-
activated K+ channel SK3 cause Zimmermann-Laband syndrome.";
Am. J. Hum. Genet. 104:1139-1157(2019).
[40]
STRUCTURE BY NMR OF 95-104.
PubMed=9927666; DOI=10.1073/pnas.96.3.903;
Siedlecka M., Goch G., Ejchart A., Sticht H., Bierzyski A.;
"Alpha-helix nucleation by a calcium-binding peptide loop.";
Proc. Natl. Acad. Sci. U.S.A. 96:903-908(1999).
[41]
STRUCTURE BY NMR OF 1-77 AND 83-149.
PubMed=11685248; DOI=10.1038/nsb1101-990;
Chou J.J., Li S., Klee C.B., Bax A.;
"Solution structure of Ca(2+)-calmodulin reveals flexible hand-like
properties of its domains.";
Nat. Struct. Biol. 8:990-997(2001).
[42] {ECO:0007744|PDB:1CLL}
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH CALCIUM, AND
CALCIUM-BINDING SITES.
PubMed=1474585; DOI=10.1016/0022-2836(92)90324-d;
Chattopadhyaya R., Meador W.E., Means A.R., Quiocho F.A.;
"Calmodulin structure refined at 1.7 A resolution.";
J. Mol. Biol. 228:1177-1192(1992).
[43]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
PubMed=7803388; DOI=10.1021/bi00255a006;
Cook W.J., Walter L.J., Walter M.R.;
"Drug binding by calmodulin: crystal structure of a calmodulin-
trifluoperazine complex.";
Biochemistry 33:15259-15265(1994).
[44]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 6-149.
PubMed=11807546; DOI=10.1038/415396a;
Drum C.L., Yan S.-Z., Bard J., Shen Y.-Q., Lu D., Soelaiman S.,
Grabarek Z., Bohm A., Tang W.-J.;
"Structural basis for the activation of anthrax adenylyl cyclase exotoxin
by calmodulin.";
Nature 415:396-402(2002).
[45]
X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1-149 IN COMPLEX WITH ANTHRAX
EDEMA FACTOR CYA.
PubMed=12485993; DOI=10.1093/emboj/cdf681;
Shen Y., Lee Y.-S., Soelaiman S., Bergson P., Lu D., Chen A.,
Beckingham K., Grabarek Z., Mrksich M., Tang W.-J.;
"Physiological calcium concentrations regulate calmodulin binding and
catalysis of adenylyl cyclase exotoxins.";
EMBO J. 21:6721-6732(2002).
[46]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MARCKS.
PubMed=12577052; DOI=10.1038/nsb900;
Yamauchi E., Nakatsu T., Matsubara M., Kato H., Taniguchi H.;
"Crystal structure of a MARCKS peptide containing the calmodulin-binding
domain in complex with Ca2+-calmodulin.";
Nat. Struct. Biol. 10:226-231(2003).
[47]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-150 IN COMPLEX WITH CACNA1C.
PubMed=16299511; DOI=10.1038/nsmb1027;
Van Petegem F., Chatelain F.C., Minor D.L. Jr.;
"Insights into voltage-gated calcium channel regulation from the structure
of the CaV1.2 IQ domain-Ca2+/calmodulin complex.";
Nat. Struct. Mol. Biol. 12:1108-1115(2005).
[48]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH ANTHRAX EDEMA FACTOR
CYA.
PubMed=15719022; DOI=10.1038/sj.emboj.7600574;
Shen Y., Zhukovskaya N.L., Guo Q., Florian J., Tang W.-J.;
"Calcium-independent calmodulin binding and two-metal-ion catalytic
mechanism of anthrax edema factor.";
EMBO J. 24:929-941(2005).
[49]
STRUCTURE BY NMR IN COMPLEX WITH SCN5A.
PubMed=21167176; DOI=10.1016/j.jmb.2010.11.046;
Chagot B., Chazin W.J.;
"Solution NMR structure of Apo-calmodulin in complex with the IQ motif of
human cardiac sodium channel NaV1.5.";
J. Mol. Biol. 406:106-119(2011).
[50]
STRUCTURE BY ELECTRON MICROSCOPY (25 ANGSTROMS) IN COMPLEX WITH MIP,
FUNCTION, AND INTERACTION WITH MIP.
PubMed=23893133; DOI=10.1038/nsmb.2630;
Reichow S.L., Clemens D.M., Freites J.A., Nemeth-Cahalan K.L., Heyden M.,
Tobias D.J., Hall J.E., Gonen T.;
"Allosteric mechanism of water-channel gating by Ca(2+)-calmodulin.";
Nat. Struct. Mol. Biol. 20:1085-1092(2013).
[51] {ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C}
X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) IN COMPLEX WITH KCNQ1 AND CALCIUM,
FUNCTION, INTERACTION WITH KCNQ1, AND DOMAIN.
PubMed=25441029; DOI=10.1016/j.str.2014.07.016;
Sachyani D., Dvir M., Strulovich R., Tria G., Tobelaim W., Peretz A.,
Pongs O., Svergun D., Attali B., Hirsch J.A.;
"Structural basis of a Kv7.1 potassium channel gating module: studies of
the intracellular c-terminal domain in complex with calmodulin.";
Structure 22:1582-1594(2014).
[52] {ECO:0007744|PDB:5J03}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM; KCNQ2 AND
KCNQ3, INTERACTION WITH KCNQ2 AND KCNQ3, AND CALCIUM-BINDING SITES.
PubMed=27564677; DOI=10.1021/acs.biochem.6b00477;
Strulovich R., Tobelaim W.S., Attali B., Hirsch J.A.;
"Structural insights into the M-channel proximal C-terminus/calmodulin
complex.";
Biochemistry 55:5353-5365(2016).
[53] {ECO:0007744|PDB:2N77}
STRUCTURE BY NMR OF 77-149 IN COMPLEX WITH PCP4, INTERACTION WITH PCP4, AND
REGION.
PubMed=27876793; DOI=10.1038/ncomms13583;
Wang X., Putkey J.A.;
"PEP-19 modulates calcium binding to calmodulin by electrostatic
steering.";
Nat. Commun. 7:13583-13583(2016).
[54]
STRUCTURE BY NMR, AND INTERACTION WITH ALPHA-SYNUCLEIN/SNCA.
PubMed=23607618; DOI=10.1021/bi400199p;
Gruschus J.M., Yap T.L., Pistolesi S., Maltsev A.S., Lee J.C.;
"NMR structure of calmodulin complexed to an N-terminally acetylated alpha-
synuclein peptide.";
Biochemistry 52:3436-3445(2013).
[55]
INTERACTION WITH LEGIONELLA PNEUMOPHILA SIDJ (MICROBIAL INFECTION), AND
FUNCTION (MICROBIAL INFECTION).
PubMed=31330532; DOI=10.1038/s41586-019-1440-8;
Bhogaraju S., Bonn F., Mukherjee R., Adams M., Pfleiderer M.M., Galej W.P.,
Matkovic V., Lopez-Mosqueda J., Kalayil S., Shin D., Dikic I.;
"Inhibition of bacterial ubiquitin ligases by SidJ-calmodulin catalysed
glutamylation.";
Nature 572:382-386(2019).
[56]
INVOLVEMENT IN CPVT4, VARIANTS CPVT4 ILE-54 AND SER-98, AND
CHARACTERIZATION OF VARIANTS CPVT4 ILE-54 AND SER-98.
PubMed=23040497; DOI=10.1016/j.ajhg.2012.08.015;
Nyegaard M., Overgaard M.T., Sondergaard M.T., Vranas M., Behr E.R.,
Hildebrandt L.L., Lund J., Hedley P.L., Camm A.J., Wettrell G., Fosdal I.,
Christiansen M., Borglum A.D.;
"Mutations in calmodulin cause ventricular tachycardia and sudden cardiac
death.";
Am. J. Hum. Genet. 91:703-712(2012).
[57]
INVOLVEMENT IN LQT14, VARIANTS LQT14 GLY-130 AND LEU-142, AND
CHARACTERIZATION OF VARIANTS LQT14 GLY-130 AND LEU-142.
PubMed=23388215; DOI=10.1161/circulationaha.112.001216;
Crotti L., Johnson C.N., Graf E., De Ferrari G.M., Cuneo B.F., Ovadia M.,
Papagiannis J., Feldkamp M.D., Rathi S.G., Kunic J.D., Pedrazzini M.,
Wieland T., Lichtner P., Beckmann B.M., Clark T., Shaffer C., Benson D.W.,
Kaab S., Meitinger T., Strom T.M., Chazin W.J., Schwartz P.J.,
George A.L. Jr.;
"Calmodulin mutations associated with recurrent cardiac arrest in
infants.";
Circulation 127:1009-1017(2013).
[58]
CHARACTERIZATION OF VARIANT LQT14 LEU-90.
PubMed=25036739; DOI=10.1016/j.febslet.2014.07.007;
Nomikos M., Thanassoulas A., Beck K., Vassilakopoulou V., Hu H.,
Calver B.L., Theodoridou M., Kashir J., Blayney L., Livaniou E.,
Rizkallah P., Nounesis G., Lai F.A.;
"Altered RyR2 regulation by the calmodulin F90L mutation associated with
idiopathic ventricular fibrillation and early sudden cardiac death.";
FEBS Lett. 588:2898-2902(2014).
[59]
INVOLVEMENT IN LQT14, AND VARIANT LQT14 LEU-90.
PubMed=24076290; DOI=10.1016/j.jacc.2013.07.091;
Marsman R.F., Barc J., Beekman L., Alders M., Dooijes D.,
van den Wijngaard A., Ratbi I., Sefiani A., Bhuiyan Z.A., Wilde A.A.,
Bezzina C.R.;
"A mutation in CALM1 encoding calmodulin in familial idiopathic ventricular
fibrillation in childhood and adolescence.";
J. Am. Coll. Cardiol. 63:259-266(2014).
[60]
VARIANTS CPVT4 ILE-54 AND SER-98, CHARACTERIZATION OF VARIANTS CPVT4 ILE-54
AND SER-98, VARIANTS LQT14 GLY-130 AND LEU-142, CHARACTERIZATION OF
VARIANTS LQT14 GLY-130 AND LEU-142, AND INTERACTION WITH RYR2.
PubMed=26164367; DOI=10.1016/j.bbagen.2015.07.001;
Vassilakopoulou V., Calver B.L., Thanassoulas A., Beck K., Hu H.,
Buntwal L., Smith A., Theodoridou M., Kashir J., Blayney L., Livaniou E.,
Nounesis G., Lai F.A., Nomikos M.;
"Distinctive malfunctions of calmodulin mutations associated with heart
RyR2-mediated arrhythmic disease.";
Biochim. Biophys. Acta 1850:2168-2176(2015).
[61]
VARIANTS CPVT4 ILE-54 AND SER-98, CHARACTERIZATION OF VARIANTS CPVT4
ILE-54; SER-98, AND INTERACTION WITH RYR2.
PubMed=27516456; DOI=10.1161/circep.116.004161;
Gomez-Hurtado N., Boczek N.J., Kryshtal D.O., Johnson C.N., Sun J.,
Nitu F.R., Cornea R.L., Chazin W.J., Calvert M.L., Tester D.J.,
Ackerman M.J., Knollmann B.C.;
"Novel CPVT-Associated Calmodulin Mutation in CALM3 (CALM3-A103V) Activates
Arrhythmogenic Ca Waves and Sparks.";
Circ. Arrhythm. Electrophysiol. 9:0-0(2016).
[62]
VARIANTS LQT14 GLY-141 AND LEU-142, CHARACTERIZATION OF VARIANT LQT14
GLY-141, AND FUNCTION.
PubMed=26969752; DOI=10.1161/circgenetics.115.001323;
Boczek N.J., Gomez-Hurtado N., Ye D., Calvert M.L., Tester D.J.,
Kryshtal D.O., Hwang H.S., Johnson C.N., Chazin W.J., Loporcaro C.G.,
Shah M., Papez A.L., Lau Y.R., Kanter R., Knollmann B.C., Ackerman M.J.;
"Spectrum and Prevalence of CALM1-, CALM2-, and CALM3-Encoded Calmodulin
Variants in Long QT Syndrome and Functional Characterization of a Novel
Long QT Syndrome-Associated Calmodulin Missense Variant, E141G.";
Circ. Cardiovasc. Genet. 9:136-146(2016).
[63]
VARIANTS CPVT4 ILE-54 AND SER-98, CHARACTERIZATION OF VARIANTS CPVT4 ILE-54
AND SER-98, VARIANTS LQT14 LEU-90 AND GLY-130, CHARACTERIZATION OF VARIANTS
LQT14 LEU-90 AND GLY-130, AND FUNCTION.
PubMed=27165696; DOI=10.1016/j.hrthm.2016.05.009;
Yu C.C., Ko J.S., Ai T., Tsai W.C., Chen Z., Rubart M., Vatta M.,
Everett T.H. IV, George A.L. Jr., Chen P.S.;
"Arrhythmogenic calmodulin mutations impede activation of small-conductance
calcium-activated potassium current.";
Heart Rhythm 13:1716-1723(2016).
[64]
CHARACTERIZATION OF VARIANT LQT14 LEU-142.
PubMed=28158429; DOI=10.1093/cvr/cvx006;
Rocchetti M., Sala L., Dreizehnter L., Crotti L., Sinnecker D., Mura M.,
Pane L.S., Altomare C., Torre E., Mostacciuolo G., Severi S., Porta A.,
De Ferrari G.M., George A.L. Jr., Schwartz P.J., Gnecchi M., Moretti A.,
Zaza A.;
"Elucidating arrhythmogenic mechanisms of long-QT syndrome CALM1-F142L
mutation in patient-specific induced pluripotent stem cell-derived
cardiomyocytes.";
Cardiovasc. Res. 113:531-541(2017).
[65]
VARIANT LQT14 VAL-141, CHARACTERIZATION OF VARIANT LQT14 VAL-141, AND
FUNCTION.
PubMed=31454269; DOI=10.1161/circgen.119.002581;
Wren L.M., Jimenez-Jaimez J., Al-Ghamdi S., Al-Aama J.Y., Bdeir A.,
Al-Hassnan Z.N., Kuan J.L., Foo R.Y., Potet F., Johnson C.N., Aziz M.C.,
Carvill G.L., Kaski J.P., Crotti L., Perin F., Monserrat L., Burridge P.W.,
Schwartz P.J., Chazin W.J., Bhuiyan Z.A., George A.L. Jr.;
"Genetic mosaicism in calmodulinopathy.";
Circ. Genom. Precis. Med. 12:375-385(2019).
-!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
ion channels, aquaporins and other proteins through calcium-binding.
Among the enzymes to be stimulated by the calmodulin-calcium complex
are a number of protein kinases and phosphatases. Together with CCP110
and centrin, is involved in a genetic pathway that regulates the
centrosome cycle and progression through cytokinesis (PubMed:16760425).
Is a regulator of voltage-dependent L-type calcium channels
(PubMed:31454269). Mediates calcium-dependent inactivation of CACNA1C
(PubMed:26969752). Positively regulates calcium-activated potassium
channel activity of KCNN2 (PubMed:27165696). Forms a potassium channel
complex with KCNQ1 and regulates electrophysiological activity of the
channel via calcium-binding (PubMed:25441029). Acts as a sensor to
modulate the endomplasmic reticulum contacts with other organelles
mediated by VMP1:ATP2A2 (PubMed:28890335).
{ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:23893133,
ECO:0000269|PubMed:26969752, ECO:0000269|PubMed:27165696,
ECO:0000269|PubMed:28890335, ECO:0000269|PubMed:31454269}.
-!- FUNCTION: (Microbial infection) Required for Legionella pneumophila
SidJ glutamylase activity. {ECO:0000269|PubMed:31330532}.
-!- SUBUNIT: Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 (By
similarity). Interacts with CEP97, CCP110, TTN/titin and SRY
(PubMed:9804419, PubMed:12871148, PubMed:15746192, PubMed:16760425,
PubMed:17719545). Interacts with USP6; the interaction is calcium
dependent (PubMed:16127172). Interacts with CDK5RAP2 (PubMed:20466722).
Interacts with SCN5A (PubMed:21167176). Interacts with RYR1
(PubMed:18650434). Interacts with FCHO1 (PubMed:22484487). Interacts
with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic
domains from two MIP subunits promotes MIP water channel closure
(PubMed:23893133). Interacts with ORAI1; this may play a role in the
regulation of ORAI1-mediated calcium transport (By similarity).
Interacts with IQCF1 (By similarity). Interacts with SYT7 (By
similarity). Interacts with CEACAM1 (via cytoplasmic domain); this
interaction is in a calcium dependent manner and reduces homophilic
cell adhesion through dissociation of dimer (By similarity). Interacts
with RYR2; regulates RYR2 calcium-release channel activity
(PubMed:27516456, PubMed:18650434, PubMed:26164367). Interacts with
PCP4; regulates calmodulin calcium-binding (PubMed:27876793). Interacts
with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is
calcium-independent, constitutive and participates in the proper
assembly of a functional heterotetrameric M channel (PubMed:27564677).
Interacts with alpha-synuclein/SNCA (PubMed:23607618). Interacts with
SLC9A1 in a calcium-dependent manner (PubMed:30287853). In the absence
of Ca(+2), interacts with GIMAP4 (via IQ domain) (By similarity).
Interacts with SCN8A; the interaction modulates the inactivation rate
of SCN8A (By similarity). Interaction with KIF1A; the interaction is
increased in presence of calcium and increases neuronal dense core
vesicles motility (PubMed:30021165). Interacts with KCNN3
(PubMed:31155282). Interacts with KCNQ1 (via C-terminus); forms a
heterooctameric structure (with 4:4 KCNQ1:CALM stoichiometry) in a
calcium-independent manner (PubMed:18165683,PubMed:25441029). Interacts
with PIK3C3; the interaction modulates PIK3C3 kinase activity
(PubMed:28890335). Interacts with HINT1; interaction increases in the
presence of calcium ions (By similarity). Interacts with HINT3 (By
similarity). {ECO:0000250|UniProtKB:P0DP26,
ECO:0000250|UniProtKB:P62157, ECO:0000250|UniProtKB:P62161,
ECO:0000250|UniProtKB:P62204, ECO:0000269|PubMed:12485993,
ECO:0000269|PubMed:12577052, ECO:0000269|PubMed:12871148,
ECO:0000269|PubMed:15719022, ECO:0000269|PubMed:15746192,
ECO:0000269|PubMed:16127172, ECO:0000269|PubMed:16299511,
ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:17719545,
ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:18650434,
ECO:0000269|PubMed:20466722, ECO:0000269|PubMed:21167176,
ECO:0000269|PubMed:22484487, ECO:0000269|PubMed:23109337,
ECO:0000269|PubMed:23607618, ECO:0000269|PubMed:23893133,
ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:26164367,
ECO:0000269|PubMed:27516456, ECO:0000269|PubMed:27564677,
ECO:0000269|PubMed:27876793, ECO:0000269|PubMed:28890335,
ECO:0000269|PubMed:30021165, ECO:0000269|PubMed:30287853,
ECO:0000269|PubMed:31155282, ECO:0000269|PubMed:9804419}.
-!- SUBUNIT: (Microbial infection) Interacts with Rubella virus
protease/methyltransferase p150. {ECO:0000269|PubMed:20086014}.
-!- SUBUNIT: (Microbial infection) Interacts with Legionella pneumophila
glutamylase SidJ. {ECO:0000269|PubMed:31330532}.
-!- INTERACTION:
P0DP23; O75874: IDH1; NbExp=7; IntAct=EBI-25817233, EBI-715695;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:14654843}.
Note=Distributed throughout the cell during interphase, but during
mitosis becomes dramatically localized to the spindle poles and the
spindle microtubules.
-!- DOMAIN: The N-terminal and C-terminal lobes of CALM bind to the C-
terminus of KCNQ1 in a clamp-like conformation. Binding of CALM C-
terminus to KCNQ1 is calcium-independent but is essential for assembly
of the structure. Binding of CALM N-terminus to KCNQ1 is calcium-
dependent and regulates electrophysiological activity of the channel.
{ECO:0000269|PubMed:25441029}.
-!- PTM: Ubiquitination results in a strongly decreased activity.
{ECO:0000250}.
-!- PTM: Phosphorylation results in a decreased activity. {ECO:0000250}.
-!- DISEASE: Ventricular tachycardia, catecholaminergic polymorphic, 4
(CPVT4) [MIM:614916]: An arrhythmogenic disorder characterized by
stress-induced, bidirectional ventricular tachycardia that may
degenerate into cardiac arrest and cause sudden death. Patients present
with recurrent syncope, seizures, or sudden death after physical
activity or emotional stress. CPVT4 inheritance is autosomal dominant.
{ECO:0000269|PubMed:23040497, ECO:0000269|PubMed:26164367,
ECO:0000269|PubMed:27165696, ECO:0000269|PubMed:27516456}. Note=The
disease is caused by variants affecting the gene represented in this
entry. Mutations in CALM1 are the cause of CPVT4.
-!- DISEASE: Long QT syndrome 14 (LQT14) [MIM:616247]: A form of long QT
syndrome, a heart disorder characterized by a prolonged QT interval on
the ECG and polymorphic ventricular arrhythmias. They cause syncope and
sudden death in response to exercise or emotional stress, and can
present with a sentinel event of sudden cardiac death in infancy.
{ECO:0000269|PubMed:23388215, ECO:0000269|PubMed:24076290,
ECO:0000269|PubMed:25036739, ECO:0000269|PubMed:26164367,
ECO:0000269|PubMed:26969752, ECO:0000269|PubMed:27165696,
ECO:0000269|PubMed:28158429, ECO:0000269|PubMed:31454269}. Note=The
disease is caused by variants affecting the gene represented in this
entry.
-!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
{ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677}.
-!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=A question of length - Issue
105 of May 2009;
URL="https://web.expasy.org/spotlight/back_issues/105";
---------------------------------------------------------------------------
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EMBL; M27319; AAA35635.1; -; mRNA.
EMBL; U12022; AAB60644.1; -; Genomic_DNA.
EMBL; U11886; AAB60644.1; JOINED; Genomic_DNA.
EMBL; BT006818; AAP35464.1; -; mRNA.
EMBL; AC006536; AAD45181.1; -; Genomic_DNA.
EMBL; AL512791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000454; AAH00454.1; -; mRNA.
EMBL; BC008597; AAH08597.1; -; mRNA.
EMBL; BC011834; AAH11834.1; -; mRNA.
EMBL; BC047523; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS9892.1; -.
PIR; S48728; MCHU.
RefSeq; NP_001316851.1; NM_001329922.1.
RefSeq; NP_001734.1; NM_001743.5.
RefSeq; NP_005175.2; NM_005184.3.
RefSeq; NP_008819.1; NM_006888.4.
PDB; 1AJI; Model; -; A=5-148.
PDB; 1CDL; X-ray; 2.00 A; A/B/C/D=2-148.
PDB; 1CLL; X-ray; 1.70 A; A=2-149.
PDB; 1CTR; X-ray; 2.45 A; A=2-149.
PDB; 1IWQ; X-ray; 2.00 A; A=2-149.
PDB; 1J7O; NMR; -; A=2-77.
PDB; 1J7P; NMR; -; A=83-149.
PDB; 1K90; X-ray; 2.75 A; D/E/F=2-149.
PDB; 1K93; X-ray; 2.95 A; D/E/F=6-149.
PDB; 1L7Z; X-ray; 2.30 A; A=2-149.
PDB; 1LVC; X-ray; 3.60 A; D/E/F=1-149.
PDB; 1NKF; NMR; -; A=94-105.
PDB; 1PK0; X-ray; 3.30 A; D/E/F=2-148.
PDB; 1S26; X-ray; 3.00 A; D/E/F=2-149.
PDB; 1SK6; X-ray; 3.20 A; D/E/F=2-149.
PDB; 1SW8; NMR; -; A=2-80.
PDB; 1UP5; X-ray; 1.90 A; A/B=2-149.
PDB; 1WRZ; X-ray; 2.00 A; A=1-149.
PDB; 1XFU; X-ray; 3.35 A; O/P/Q/R/S/T=1-149.
PDB; 1XFV; X-ray; 3.35 A; O/P/Q/R/S/T=1-149.
PDB; 1XFW; X-ray; 3.40 A; O/P/Q/R/S/T=1-149.
PDB; 1XFX; X-ray; 3.20 A; O/P/Q/R/S/T=1-149.
PDB; 1XFY; X-ray; 3.30 A; O/P/Q/R/S/T=1-149.
PDB; 1XFZ; X-ray; 3.25 A; O/P/Q/R/S/T=1-149.
PDB; 1Y6W; X-ray; 2.40 A; A=2-149.
PDB; 1YR5; X-ray; 1.70 A; A=2-149.
PDB; 1YRT; X-ray; 2.10 A; B=76-149.
PDB; 1YRU; X-ray; 2.50 A; B=76-149.
PDB; 1ZOT; X-ray; 2.20 A; B=80-148.
PDB; 1ZUZ; X-ray; 1.91 A; A=1-149.
PDB; 2BE6; X-ray; 2.00 A; A/B/C=1-149.
PDB; 2F3Y; X-ray; 1.45 A; A=2-149.
PDB; 2F3Z; X-ray; 1.60 A; A=2-149.
PDB; 2HF5; NMR; -; A=47-114.
PDB; 2I08; X-ray; 2.00 A; A=3-79.
PDB; 2JZI; NMR; -; A=2-149.
PDB; 2K0E; NMR; -; A=2-149.
PDB; 2K0F; NMR; -; A=2-149.
PDB; 2K0J; NMR; -; A=3-149.
PDB; 2K61; NMR; -; A=2-149.
PDB; 2KNE; NMR; -; A=2-149.
PDB; 2KUG; NMR; -; A=2-77.
PDB; 2KUH; NMR; -; A=83-149.
PDB; 2L53; NMR; -; A=2-149.
PDB; 2L7L; NMR; -; A=2-149.
PDB; 2LGF; NMR; -; A=3-149.
PDB; 2LL6; NMR; -; A=2-149.
PDB; 2LL7; NMR; -; A=2-149.
PDB; 2LQC; NMR; -; A=2-78.
PDB; 2LQP; NMR; -; A=79-149.
PDB; 2LV6; Other; -; A=2-149.
PDB; 2M0J; NMR; -; A=2-149.
PDB; 2M0K; NMR; -; A=2-149.
PDB; 2M55; NMR; -; A=2-149.
PDB; 2MG5; NMR; -; A=2-149.
PDB; 2N27; NMR; -; A=2-149.
PDB; 2N6A; NMR; -; A=6-147.
PDB; 2N77; NMR; -; A=77-149.
PDB; 2N8J; NMR; -; A=2-149.
PDB; 2R28; X-ray; 1.86 A; A/B=1-149.
PDB; 2V01; X-ray; 2.15 A; A=2-149.
PDB; 2V02; X-ray; 2.20 A; A=2-149.
PDB; 2VAY; X-ray; 1.94 A; A=4-149.
PDB; 2W73; X-ray; 1.45 A; A/B/E/F=1-149.
PDB; 2WEL; X-ray; 1.90 A; D=1-149.
PDB; 2X0G; X-ray; 2.20 A; B=2-149.
PDB; 2Y4V; X-ray; 1.80 A; A=1-149.
PDB; 3BYA; X-ray; 1.85 A; A=2-149.
PDB; 3DVE; X-ray; 2.35 A; A=2-149.
PDB; 3DVJ; X-ray; 2.80 A; A=2-149.
PDB; 3DVK; X-ray; 2.30 A; A=2-149.
PDB; 3DVM; X-ray; 2.60 A; A=2-149.
PDB; 3EWT; X-ray; 2.40 A; A=2-149.
PDB; 3EWV; X-ray; 2.60 A; A=2-149.
PDB; 3G43; X-ray; 2.10 A; A/B/C/D=2-149.
PDB; 3HR4; X-ray; 2.50 A; B/D/F/H=1-149.
PDB; 3J41; EM; 25.0 A; E/F=1-149.
PDB; 3O77; X-ray; 2.35 A; A=1-149.
PDB; 3O78; X-ray; 2.60 A; A/B=1-149.
PDB; 3OXQ; X-ray; 2.55 A; A/B/C/D=1-149.
PDB; 3SUI; X-ray; 1.95 A; A=1-149.
PDB; 3UCT; X-ray; 1.90 A; A/B=2-80.
PDB; 3UCW; X-ray; 1.76 A; A/B/C/D=2-80.
PDB; 3UCY; X-ray; 1.80 A; A=2-80.
PDB; 4BW7; X-ray; 1.81 A; A/C=1-149.
PDB; 4BW8; X-ray; 1.80 A; A/B=1-149.
PDB; 4BYF; X-ray; 2.74 A; B/D=1-149.
PDB; 4DCK; X-ray; 2.20 A; B=1-149.
PDB; 4DJC; X-ray; 1.35 A; A=1-149.
PDB; 4GOW; X-ray; 2.60 A; D=4-147.
PDB; 4JPZ; X-ray; 3.02 A; C/I=1-149.
PDB; 4JQ0; X-ray; 3.84 A; C=1-149.
PDB; 4L79; X-ray; 2.30 A; B=1-149.
PDB; 4LZX; X-ray; 1.50 A; A=2-149.
PDB; 4M1L; X-ray; 2.10 A; A=2-149.
PDB; 4OVN; X-ray; 2.80 A; A/B/C/D/E=1-149.
PDB; 4Q57; X-ray; 1.80 A; A=10-74.
PDB; 4Q5U; X-ray; 1.95 A; A=1-149.
PDB; 4UMO; X-ray; 3.00 A; C/D=1-149.
PDB; 4UPU; X-ray; 2.34 A; A=2-149.
PDB; 4V0C; X-ray; 2.86 A; C/D=1-149.
PDB; 5COC; X-ray; 2.67 A; A=5-78.
PDB; 5DBR; X-ray; 2.25 A; A=5-149.
PDB; 5DOW; X-ray; 1.70 A; A/C/E/G=2-149.
PDB; 5DSU; X-ray; 1.93 A; A=3-78.
PDB; 5GGM; NMR; -; A=2-149.
PDB; 5I0I; X-ray; 3.15 A; C/E=3-147, G=84-126, I=84-147.
PDB; 5J03; X-ray; 2.00 A; B=1-149.
PDB; 5J8H; NMR; -; A=2-149.
PDB; 5JQA; X-ray; 1.80 A; A=1-149.
PDB; 5JTH; X-ray; 1.84 A; A=1-149.
PDB; 5K7L; EM; 3.78 A; B=1-149.
PDB; 5K8Q; X-ray; 1.74 A; A=1-149.
PDB; 5OEO; NMR; -; A=1-149.
PDB; 5TP5; NMR; -; A=2-149.
PDB; 5TP6; NMR; -; A=2-149.
PDB; 5V02; X-ray; 1.78 A; R=1-149.
PDB; 5V03; X-ray; 1.58 A; R=1-149.
PDB; 5V7X; X-ray; 3.14 A; B=1-149.
PDB; 5WBX; X-ray; 1.90 A; R=5-148.
PDB; 5WC5; X-ray; 2.30 A; R=5-148.
PDB; 6B8L; X-ray; 2.30 A; B/D/F/H=1-149.
PDB; 6B8M; X-ray; 2.30 A; B/D/F/H=1-149.
PDB; 6B8N; X-ray; 2.20 A; B/D/F/H=1-149.
PDB; 6B8P; X-ray; 2.20 A; B/D/F/H=1-149.
PDB; 6B8Q; X-ray; 2.60 A; B/D/F/H=1-149.
PDB; 6BUT; NMR; -; A=2-149.
PDB; 6C1D; EM; 3.20 A; R=2-149.
PDB; 6C1G; EM; 3.80 A; R=2-149.
PDB; 6C1H; EM; 3.90 A; R=2-149.
PDB; 6CNM; EM; 3.40 A; E/F/G/H=1-149.
PDB; 6CNN; EM; 3.50 A; E/F/G/H=1-149.
PDB; 6CNO; EM; 4.70 A; E/F/G/H=1-149.
PDB; 6DAD; X-ray; 1.65 A; A/B=2-149.
PDB; 6DAE; X-ray; 2.00 A; A/B=2-149.
PDB; 6DAF; X-ray; 2.40 A; A/B=2-149.
PDB; 6DAH; X-ray; 2.50 A; A/B/C/D=1-149.
PDB; 6E2F; EM; 3.90 A; E=1-149.
PDB; 6E2G; EM; 3.60 A; E=1-149.
PDB; 6EEB; X-ray; 1.96 A; A=1-149.
PDB; 6FEG; NMR; -; B=1-149.
PDB; 6FEH; NMR; -; B=1-149.
PDB; 6GDK; NMR; -; A=2-149.
PDB; 6GDL; NMR; -; A=2-80.
PDB; 6HCS; X-ray; 2.00 A; A/C/E/G=1-149.
PDB; 6HR1; X-ray; 1.90 A; A/B=2-149.
PDB; 6JI8; EM; 3.60 A; C/F/I/L=1-149.
PDB; 6JII; EM; 4.20 A; C/F/I/L=1-149.
PDB; 6JIU; EM; 4.20 A; C/F/I/L=1-149.
PDB; 6JIY; EM; 3.90 A; C/F/I/L=1-149.
PDB; 6JRS; EM; 3.70 A; C/F/I/L=1-149.
PDB; 6JV2; EM; 4.40 A; B/D/F/H=1-149.
PDB; 6K4K; X-ray; 2.71 A; C/D=1-149.
PDB; 6K4L; X-ray; 2.95 A; C/D=1-149.
PDB; 6K4R; X-ray; 3.11 A; C/D=1-149.
PDB; 6M2W; EM; 3.80 A; C/F/I/L=1-149.
PDB; 6M7H; X-ray; 1.60 A; A=2-148.
PDB; 6MUD; X-ray; 2.69 A; A=1-149.
PDB; 6MUE; X-ray; 1.90 A; A=1-149.
PDB; 6N5W; X-ray; 2.15 A; C=1-149.
PDB; 6O5G; X-ray; 1.89 A; A=1-149.
PDB; 6OS4; X-ray; 2.05 A; A=2-149.
PDB; 6PAW; X-ray; 2.95 A; C/D/G/H=1-149.
PDB; 6PBX; EM; 4.00 A; B/D/F/H=1-149.
PDB; 6PBY; EM; 3.67 A; B/D/F/H=1-149.
PDB; 6U39; X-ray; 2.40 A; A/C/E/G/I/K/M/O/Q/S=2-149.
PDB; 6U3A; X-ray; 1.65 A; A/B=2-149.
PDB; 6U3B; X-ray; 1.70 A; A=2-149.
PDB; 6U3D; X-ray; 1.75 A; A/B=2-149.
PDB; 6UZZ; EM; 3.10 A; B/D/F/H=1-149.
PDB; 6V00; EM; 3.10 A; B/E/H/K=1-149.
PDB; 6V01; EM; 3.90 A; B/E/H/K=1-149.
PDB; 6X32; EM; 3.80 A; C/F/I/L=3-148.
PDB; 6X33; EM; 4.20 A; C/F/I/L=1-148.
PDB; 6X35; EM; 4.20 A; C/F/I/L=1-148.
PDB; 6X36; EM; 4.70 A; C/F/I/L=1-148.
PDB; 6XXX; X-ray; 1.25 A; AAA=1-149.
PDB; 6XY3; X-ray; 2.00 A; AAA=1-149.
PDB; 6XYR; X-ray; 2.08 A; A=2-149.
PDB; 6Y4P; X-ray; 2.13 A; A=1-149.
PDB; 6Y94; NMR; -; A=2-149.
PDB; 6Y95; NMR; -; A=2-149.
PDB; 6YNS; X-ray; 3.94 A; A/B/C/D/E/F/G/H/I/J/K/L=2-149.
PDB; 6YNU; X-ray; 3.12 A; A/C=2-149.
PDB; 6ZBI; NMR; -; A=2-149.
PDB; 7KL5; X-ray; 1.65 A; A=1-149.
PDBsum; 1AJI; -.
PDBsum; 1CDL; -.
PDBsum; 1CLL; -.
PDBsum; 1CTR; -.
PDBsum; 1IWQ; -.
PDBsum; 1J7O; -.
PDBsum; 1J7P; -.
PDBsum; 1K90; -.
PDBsum; 1K93; -.
PDBsum; 1L7Z; -.
PDBsum; 1LVC; -.
PDBsum; 1NKF; -.
PDBsum; 1PK0; -.
PDBsum; 1S26; -.
PDBsum; 1SK6; -.
PDBsum; 1SW8; -.
PDBsum; 1UP5; -.
PDBsum; 1WRZ; -.
PDBsum; 1XFU; -.
PDBsum; 1XFV; -.
PDBsum; 1XFW; -.
PDBsum; 1XFX; -.
PDBsum; 1XFY; -.
PDBsum; 1XFZ; -.
PDBsum; 1Y6W; -.
PDBsum; 1YR5; -.
PDBsum; 1YRT; -.
PDBsum; 1YRU; -.
PDBsum; 1ZOT; -.
PDBsum; 1ZUZ; -.
PDBsum; 2BE6; -.
PDBsum; 2F3Y; -.
PDBsum; 2F3Z; -.
PDBsum; 2HF5; -.
PDBsum; 2I08; -.
PDBsum; 2JZI; -.
PDBsum; 2K0E; -.
PDBsum; 2K0F; -.
PDBsum; 2K0J; -.
PDBsum; 2K61; -.
PDBsum; 2KNE; -.
PDBsum; 2KUG; -.
PDBsum; 2KUH; -.
PDBsum; 2L53; -.
PDBsum; 2L7L; -.
PDBsum; 2LGF; -.
PDBsum; 2LL6; -.
PDBsum; 2LL7; -.
PDBsum; 2LQC; -.
PDBsum; 2LQP; -.
PDBsum; 2LV6; -.
PDBsum; 2M0J; -.
PDBsum; 2M0K; -.
PDBsum; 2M55; -.
PDBsum; 2MG5; -.
PDBsum; 2N27; -.
PDBsum; 2N6A; -.
PDBsum; 2N77; -.
PDBsum; 2N8J; -.
PDBsum; 2R28; -.
PDBsum; 2V01; -.
PDBsum; 2V02; -.
PDBsum; 2VAY; -.
PDBsum; 2W73; -.
PDBsum; 2WEL; -.
PDBsum; 2X0G; -.
PDBsum; 2Y4V; -.
PDBsum; 3BYA; -.
PDBsum; 3DVE; -.
PDBsum; 3DVJ; -.
PDBsum; 3DVK; -.
PDBsum; 3DVM; -.
PDBsum; 3EWT; -.
PDBsum; 3EWV; -.
PDBsum; 3G43; -.
PDBsum; 3HR4; -.
PDBsum; 3J41; -.
PDBsum; 3O77; -.
PDBsum; 3O78; -.
PDBsum; 3OXQ; -.
PDBsum; 3SUI; -.
PDBsum; 3UCT; -.
PDBsum; 3UCW; -.
PDBsum; 3UCY; -.
PDBsum; 4BW7; -.
PDBsum; 4BW8; -.
PDBsum; 4BYF; -.
PDBsum; 4DCK; -.
PDBsum; 4DJC; -.
PDBsum; 4GOW; -.
PDBsum; 4JPZ; -.
PDBsum; 4JQ0; -.
PDBsum; 4L79; -.
PDBsum; 4LZX; -.
PDBsum; 4M1L; -.
PDBsum; 4OVN; -.
PDBsum; 4Q57; -.
PDBsum; 4Q5U; -.
PDBsum; 4UMO; -.
PDBsum; 4UPU; -.
PDBsum; 4V0C; -.
PDBsum; 5COC; -.
PDBsum; 5DBR; -.
PDBsum; 5DOW; -.
PDBsum; 5DSU; -.
PDBsum; 5GGM; -.
PDBsum; 5I0I; -.
PDBsum; 5J03; -.
PDBsum; 5J8H; -.
PDBsum; 5JQA; -.
PDBsum; 5JTH; -.
PDBsum; 5K7L; -.
PDBsum; 5K8Q; -.
PDBsum; 5OEO; -.
PDBsum; 5TP5; -.
PDBsum; 5TP6; -.
PDBsum; 5V02; -.
PDBsum; 5V03; -.
PDBsum; 5V7X; -.
PDBsum; 5WBX; -.
PDBsum; 5WC5; -.
PDBsum; 6B8L; -.
PDBsum; 6B8M; -.
PDBsum; 6B8N; -.
PDBsum; 6B8P; -.
PDBsum; 6B8Q; -.
PDBsum; 6BUT; -.
PDBsum; 6C1D; -.
PDBsum; 6C1G; -.
PDBsum; 6C1H; -.
PDBsum; 6CNM; -.
PDBsum; 6CNN; -.
PDBsum; 6CNO; -.
PDBsum; 6DAD; -.
PDBsum; 6DAE; -.
PDBsum; 6DAF; -.
PDBsum; 6DAH; -.
PDBsum; 6E2F; -.
PDBsum; 6E2G; -.
PDBsum; 6EEB; -.
PDBsum; 6FEG; -.
PDBsum; 6FEH; -.
PDBsum; 6GDK; -.
PDBsum; 6GDL; -.
PDBsum; 6HCS; -.
PDBsum; 6HR1; -.
PDBsum; 6JI8; -.
PDBsum; 6JII; -.
PDBsum; 6JIU; -.
PDBsum; 6JIY; -.
PDBsum; 6JRS; -.
PDBsum; 6JV2; -.
PDBsum; 6K4K; -.
PDBsum; 6K4L; -.
PDBsum; 6K4R; -.
PDBsum; 6M2W; -.
PDBsum; 6M7H; -.
PDBsum; 6MUD; -.
PDBsum; 6MUE; -.
PDBsum; 6N5W; -.
PDBsum; 6O5G; -.
PDBsum; 6OS4; -.
PDBsum; 6PAW; -.
PDBsum; 6PBX; -.
PDBsum; 6PBY; -.
PDBsum; 6U39; -.
PDBsum; 6U3A; -.
PDBsum; 6U3B; -.
PDBsum; 6U3D; -.
PDBsum; 6UZZ; -.
PDBsum; 6V00; -.
PDBsum; 6V01; -.
PDBsum; 6X32; -.
PDBsum; 6X33; -.
PDBsum; 6X35; -.
PDBsum; 6X36; -.
PDBsum; 6XXX; -.
PDBsum; 6XY3; -.
PDBsum; 6XYR; -.
PDBsum; 6Y4P; -.
PDBsum; 6Y94; -.
PDBsum; 6Y95; -.
PDBsum; 6YNS; -.
PDBsum; 6YNU; -.
PDBsum; 6ZBI; -.
PDBsum; 7KL5; -.
SASBDB; P0DP23; -.
SMR; P0DP23; -.
IntAct; P0DP23; 4.
MINT; P0DP23; -.
STRING; 9606.ENSP00000349467; -.
BindingDB; P0DP23; -.
ChEMBL; CHEMBL6093; -.
DrugBank; DB08039; (3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDE.
DrugBank; DB01429; Aprindine.
DrugBank; DB01244; Bepridil.
DrugBank; DB01373; Calcium.
DrugBank; DB11093; Calcium citrate.
DrugBank; DB13800; Calcium levulinate.
DrugBank; DB11348; Calcium Phosphate.
DrugBank; DB14481; Calcium phosphate dihydrate.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB00527; Cinchocaine.
DrugBank; DB02868; Deacetoxyvinzolidine.
DrugBank; DB01023; Felodipine.
DrugBank; DB04841; Flunarizine.
DrugBank; DB00623; Fluphenazine.
DrugBank; DB00753; Isoflurane.
DrugBank; DB00836; Loperamide.
DrugBank; DB01065; Melatonin.
DrugBank; DB08231; Myristic acid.
DrugBank; DB04513; N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide.
DrugBank; DB00622; Nicardipine.
DrugBank; DB01115; Nifedipine.
DrugBank; DB00850; Perphenazine.
DrugBank; DB00925; Phenoxybenzamine.
DrugBank; DB01100; Pimozide.
DrugBank; DB04825; Prenylamine.
DrugBank; DB01069; Promethazine.
DrugBank; DB03900; tert-butanol.
DrugBank; DB00831; Trifluoperazine.
DrugBank; DB03977; Trimethyllysine.
DrugCentral; P0DP23; -.
MoonDB; P0DP23; Predicted.
GlyGen; P0DP23; 1 site, 1 O-linked glycan (1 site).
iPTMnet; P0DP23; -.
MetOSite; P0DP23; -.
PhosphoSitePlus; P0DP23; -.
BioMuta; CALM1; -.
jPOST; P0DP23; -.
MassIVE; P0DP23; -.
PeptideAtlas; P0DP23; -.
PRIDE; P0DP23; -.
Antibodypedia; 4344; 534 antibodies.
DNASU; 801; -.
Ensembl; ENST00000356978; ENSP00000349467; ENSG00000198668.
GeneID; 801; -.
GeneID; 805; -.
GeneID; 808; -.
KEGG; hsa:801; -.
KEGG; hsa:805; -.
KEGG; hsa:808; -.
CTD; 801; -.
CTD; 805; -.
CTD; 808; -.
DisGeNET; 801; -.
DisGeNET; 805; -.
DisGeNET; 808; -.
GeneCards; CALM1; -.
GeneReviews; CALM1; -.
HGNC; HGNC:1442; CALM1.
HPA; ENSG00000198668; Tissue enhanced (brain).
MalaCards; CALM1; -.
MIM; 114180; gene.
MIM; 614916; phenotype.
MIM; 616247; phenotype.
neXtProt; NX_P0DP23; -.
OpenTargets; ENSG00000143933; -.
OpenTargets; ENSG00000160014; -.
OpenTargets; ENSG00000198668; -.
VEuPathDB; HostDB:ENSG00000198668; -.
eggNOG; KOG0027; Eukaryota.
OMA; RTCPSHL; -.
OrthoDB; 1386217at2759; -.
PathwayCommons; P0DP23; -.
Reactome; R-HSA-111932; CaMK IV-mediated phosphorylation of CREB.
Reactome; R-HSA-111933; Calmodulin induced events.
Reactome; R-HSA-111957; Cam-PDE 1 activation.
Reactome; R-HSA-111997; CaM pathway.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
Reactome; R-HSA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-HSA-163615; PKA activation.
Reactome; R-HSA-180024; DARPP-32 events.
Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-HSA-2025928; Calcineurin activates NFAT.
Reactome; R-HSA-203615; eNOS activation.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-HSA-425561; Sodium/Calcium exchangers.
Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
Reactome; R-HSA-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
Reactome; R-HSA-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
Reactome; R-HSA-8876725; Protein methylation.
Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
Reactome; R-HSA-9022535; Loss of phosphorylation of MECP2 at T308.
Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission.
Reactome; R-HSA-9619229; Activation of RAC1 downstream of NMDARs.
Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs.
Reactome; R-HSA-9620244; Long-term potentiation.
Reactome; R-HSA-9648002; RAS processing.
Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
BioGRID-ORCS; 801; 3 hits in 1016 CRISPR screens.
BioGRID-ORCS; 805; 32 hits in 910 CRISPR screens.
BioGRID-ORCS; 808; 39 hits in 1011 CRISPR screens.
ChiTaRS; CALM1; human.
Pharos; P0DP23; Tclin.
PRO; PR:P0DP23; -.
Proteomes; UP000005640; Chromosome 14.
RNAct; P0DP23; protein.
ExpressionAtlas; P0DP23; baseline and differential.
GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
GO; GO:1902494; C:catalytic complex; IDA:CAFA.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0030017; C:sarcomere; IDA:BHF-UCL.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
GO; GO:0010856; F:adenylate cyclase activator activity; IDA:UniProtKB.
GO; GO:0008179; F:adenylate cyclase binding; IPI:CAFA.
GO; GO:0019855; F:calcium channel inhibitor activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
GO; GO:0031997; F:N-terminal myristoylation domain binding; IPI:UniProtKB.
GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; IEA:Ensembl.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0072542; F:protein phosphatase activator activity; IDA:BHF-UCL.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; TAS:BHF-UCL.
GO; GO:0031432; F:titin binding; IPI:BHF-UCL.
GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
GO; GO:0031800; F:type 3 metabotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0007190; P:activation of adenylate cyclase activity; IEA:Ensembl.
GO; GO:0016240; P:autophagosome membrane docking; IDA:UniProtKB.
GO; GO:0005513; P:detection of calcium ion; IMP:BHF-UCL.
GO; GO:0090151; P:establishment of protein localization to mitochondrial membrane; IEA:Ensembl.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IDA:UniProtKB.
GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; IEA:Ensembl.
GO; GO:1901842; P:negative regulation of high voltage-gated calcium channel activity; IMP:UniProtKB.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; TAS:BHF-UCL.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:UniProtKB.
GO; GO:0140056; P:organelle localization by membrane tethering; IDA:UniProtKB.
GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IDA:BHF-UCL.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; TAS:BHF-UCL.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; TAS:BHF-UCL.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:BHF-UCL.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; TAS:BHF-UCL.
GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0050848; P:regulation of calcium-mediated signaling; IEA:Ensembl.
GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IMP:UniProtKB.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL.
GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IC:BHF-UCL.
GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IDA:UniProtKB.
GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
CDD; cd00051; EFh; 2.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 2.
SMART; SM00054; EFh; 4.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 4.
PROSITE; PS50222; EF_HAND_2; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Disease variant; Host-virus interaction;
Isopeptide bond; Long QT syndrome; Metal-binding; Methylation;
Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7,
ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
CHAIN 2..149
/note="Calmodulin-1"
/id="PRO_0000439932"
DOMAIN 8..43
/note="EF-hand 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
DOMAIN 44..79
/note="EF-hand 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
DOMAIN 81..116
/note="EF-hand 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
DOMAIN 117..149
/note="EF-hand 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
CA_BIND 21..32
/note="1"
/evidence="ECO:0000269|PubMed:1474585,
ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677,
ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO,
ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03"
CA_BIND 57..68
/note="2"
/evidence="ECO:0000269|PubMed:1474585,
ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677,
ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO,
ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03"
CA_BIND 94..105
/note="3"
/evidence="ECO:0000269|PubMed:1474585,
ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL,
ECO:0007744|PDB:5J03"
CA_BIND 130..141
/note="4"
/evidence="ECO:0000269|PubMed:1474585,
ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL,
ECO:0007744|PDB:5J03"
REGION 77..149
/note="Necessary and sufficient for interaction with PCP4"
/evidence="ECO:0000269|PubMed:27876793"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7,
ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
MOD_RES 22
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 45
/note="Phosphothreonine; by CaMK4"
/evidence="ECO:0000250|UniProtKB:P0DP29"
MOD_RES 82
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 95
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 100
/note="Phosphotyrosine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332"
MOD_RES 102
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 111
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 116
/note="N6,N6,N6-trimethyllysine; alternate"
/evidence="ECO:0000269|PubMed:7093203,
ECO:0007744|PubMed:24129315"
MOD_RES 116
/note="N6-methyllysine; alternate"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 139
/note="Phosphotyrosine"
/evidence="ECO:0007744|PubMed:19690332"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000250|UniProtKB:P62157"
VARIANT 54
/note="N -> I (in CPVT4; increased RYR2 calcium-release
channel activity; not changed calcium-dependent
inactivation of L-type calcium channel; not changed protein
abundance; not changed structure; not changed thermal
stability both in the absence and presence of calcium; no
effect on the calcium binding affinity; significantly
increased binding of RYR2; increased ryanodine-sensitive
calcium-release channel activity; decreased of KCNN2
calcium-activated potassium channel activity; not changed
KCNN2 expression; not changed KCNN2 location at membrane;
dbSNP:rs267607276)"
/evidence="ECO:0000269|PubMed:23040497,
ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:27165696,
ECO:0000269|PubMed:27516456"
/id="VAR_069222"
VARIANT 90
/note="F -> L (in LQT14; significantly decreased of KCNN2
calcium-activated potassium channel activity; not changed
KCNN2 expression; not changed KCNN2 location at membrane;
decreased thermal stability in presence of calcium ions;
decreased interaction with RYR2; dbSNP:rs730882253)"
/evidence="ECO:0000269|PubMed:24076290,
ECO:0000269|PubMed:25036739, ECO:0000269|PubMed:27165696"
/id="VAR_073275"
VARIANT 98
/note="N -> S (in CPVT4; the mutant has significantly
reduced calcium affinity compared to wild-type; calmodulin-
RYR2 interaction is defective at low intracellular Ca(2+)
concentrations and restored at moderate to high Ca(2+)
concentrations; increased RYR2 calcium-release channel
activity; decreased KCNN2 calcium-activated potassium
channel activity; not changed KCNN2 expression; not changed
KCNN2 location at membrane; dbSNP:rs267607277)"
/evidence="ECO:0000269|PubMed:23040497,
ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:27165696,
ECO:0000269|PubMed:27516456"
/id="VAR_078541"
VARIANT 130
/note="D -> G (in LQT14; reduction in calcium affinity; not
changed protein abundance; not changed structure;
significantly decreased thermal stability in presence of
calcium; significantly decreased RYR2 interaction;
increased ryanodine-sensitive calcium-release channel
activity; decreased of KCNN2 calcium-activated potassium
channel activity; not changed KCNN2 expression; not changed
KCNN2 location at membrane; dbSNP:rs730882252)"
/evidence="ECO:0000269|PubMed:23388215,
ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:27165696"
/id="VAR_078542"
VARIANT 141
/note="E -> G (in LQT14; decreased calcium affinity; loss
of CACNA1C calcium-dependent-inactivation; no effect on
intracellular RYR2-mediated calcium release)"
/evidence="ECO:0000269|PubMed:26969752"
/id="VAR_078263"
VARIANT 141
/note="E -> V (in LQT14; loss-of-function variant causing
impaired negative regulation of high voltage-gated calcium
channel activity; impaired regulation of cardiac muscle
cell action potential; decreased calcium ion binding)"
/evidence="ECO:0000269|PubMed:31454269"
/id="VAR_083814"
VARIANT 142
/note="F -> L (in LQT14; reduction in calcium affinity; not
changed protein abundance; not changed structure;
significantly decreased thermal stability in presence of
calcium; no effect on RYR2 interaction; significantly
reduced ryanodine-sensitive calcium-release channel
activity; impaired negative regulation of high voltage-
gated calcium channel activity; impaired regulation of
cardiac muscle cell action potential; dbSNP:rs1085307479
and dbSNP:rs199744595)"
/evidence="ECO:0000269|PubMed:23388215,
ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:26969752,
ECO:0000269|PubMed:28158429"
/id="VAR_073282"
HELIX 2..4
/evidence="ECO:0007829|PDB:4DJC"
HELIX 7..20
/evidence="ECO:0007829|PDB:4DJC"
STRAND 21..23
/evidence="ECO:0007829|PDB:2M0J"
STRAND 25..28
/evidence="ECO:0007829|PDB:4DJC"
HELIX 30..39
/evidence="ECO:0007829|PDB:4DJC"
HELIX 46..56
/evidence="ECO:0007829|PDB:4DJC"
HELIX 57..59
/evidence="ECO:0007829|PDB:4LZX"
STRAND 61..65
/evidence="ECO:0007829|PDB:4DJC"
HELIX 66..93
/evidence="ECO:0007829|PDB:4DJC"
STRAND 94..96
/evidence="ECO:0007829|PDB:1WRZ"
STRAND 97..101
/evidence="ECO:0007829|PDB:4DJC"
HELIX 103..112
/evidence="ECO:0007829|PDB:4DJC"
STRAND 113..115
/evidence="ECO:0007829|PDB:4LZX"
HELIX 119..129
/evidence="ECO:0007829|PDB:4DJC"
TURN 130..132
/evidence="ECO:0007829|PDB:4DCK"
STRAND 133..138
/evidence="ECO:0007829|PDB:4DJC"
HELIX 139..146
/evidence="ECO:0007829|PDB:4DJC"
SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK


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WP1347: Triacylglyceride Synthesis
WP163: Cytoplasmic Ribosomal Proteins
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Related Genes :
[Camkk1 Camkk] Calcium/calmodulin-dependent protein kinase kinase 1 (CaM-KK 1) (CaM-kinase kinase 1) (CaMKK 1) (EC 2.7.11.17) (CaM-kinase IV kinase) (Calcium/calmodulin-dependent protein kinase kinase alpha) (CaM-KK alpha) (CaM-kinase kinase alpha) (CaMKK alpha)
[cya cyaA BP0760] Bifunctional hemolysin/adenylate cyclase (AC-HLY) (ACT) (Cyclolysin) [Cleaved into: Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase); Hemolysin]
[cya pXO1-122 BXA0141 GBAA_pXO1_0142] Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Anthrax edema toxin adenylate cyclase component) (Edema factor) (EF)
[CAMTA3 CMTA3 SARD3 SR1 At2g22300 T26C19.4] Calmodulin-binding transcription activator 3 (AtCAMTA3) (Ethylene-induced calmodulin-binding protein 1) (EICBP1) (Ethylene-induced calmodulin-binding protein a) (EICBP.a) (Protein SAR-DEFICIENT 3) (Signal-responsive protein 1) (AtSR1)
[Ppp3ca Calna] Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform) (CNA alpha)
[Camkk1] Calcium/calmodulin-dependent protein kinase kinase 1 (CaM-KK 1) (CaM-kinase kinase 1) (CaMKK 1) (EC 2.7.11.17) (CaM-kinase IV kinase) (Calcium/calmodulin-dependent protein kinase kinase alpha) (CaM-KK alpha) (CaM-kinase kinase alpha) (CaMKK alpha)
[CAMKK1 CAMKKA] Calcium/calmodulin-dependent protein kinase kinase 1 (CaM-KK 1) (CaM-kinase kinase 1) (CaMKK 1) (EC 2.7.11.17) (CaM-kinase IV kinase) (Calcium/calmodulin-dependent protein kinase kinase alpha) (CaM-KK alpha) (CaM-kinase kinase alpha) (CaMKK alpha)
[CAMTA1 CMTA1 SR2 At5g09410 T5E8.210] Calmodulin-binding transcription activator 1 (AtCAMTA1) (Ethylene-induced calmodulin-binding protein b) (EICBP.b) (Signal-responsive protein 2) (AtSR2)
[CRK1 CaMK3 CBK3 At2g41140 T3K9.9] CDPK-related kinase 1 (AtCRK1) (EC 2.7.11.1) (Calcium/calmodulin-dependent protein kinase 3) (Calmodulin-binding protein kinase 3) (AtCBK3) (CaM-binding protein kinase 3)
[Aspm Calmbp1 Sha1] Abnormal spindle-like microcephaly-associated protein homolog (Calmodulin-binding protein Sha1) (Calmodulin-binding protein 1) (Spindle and hydroxyurea checkpoint abnormal protein)
[CAMK1 Os03g0366200 LOC_Os03g25070] Calcium/calmodulin-dependent serine/threonine-protein kinase 1 (EC 2.7.11.17) (Calcium/calmodulin-binding serine/threonine-protein kinase) (CaM-binding protein kinase) (OsCBK)
[CAMTA2 CMTA2 SR4 At5g64220 MSJ1.6] Calmodulin-binding transcription activator 2 (AtCAMTA2) (AtER66) (Ethylene-induced calmodulin-binding protein c) (EICBP.c) (Signal-responsive protein 4) (AtSR4)
[CAMRLK MEE62 At5g45800 MRA19.24] Calmodulin-binding receptor kinase CaMRLK (EC 2.7.11.1) (Calmodulin-binding receptor-like kinase) (AtCaMRLK) (Protein MATERNAL EFFECT EMBRYO ARREST 62)
[Camk2n1] Calcium/calmodulin-dependent protein kinase II inhibitor 1 (calcium/calmodulin-dependent protein kinase II inhibitor alpha) (CaM-KIINalpha) (CaMKIINalpha)
[CAMSAP2 CAMSAP1L1 KIAA1078] Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)
[Camsap2 Camsap1l1 Kiaa1078] Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)
[CML24 TCH2 At5g37770 K22F20.1] Calcium-binding protein CML24 (Calmodulin-like protein 24) (Touch-induced calmodulin-related protein 2)
[Camk2a] Calcium/calmodulin-dependent protein kinase type II subunit alpha (CaM kinase II subunit alpha) (CaMK-II subunit alpha) (EC 2.7.11.17)
[Camk2b Camk2d] Calcium/calmodulin-dependent protein kinase type II subunit beta (CaM kinase II subunit beta) (CaMK-II subunit beta) (EC 2.7.11.17)
[Camk1] Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (CaM kinase I alpha) (CaMKI-alpha)
[ADCY1] Adenylate cyclase type 1 (EC 4.6.1.1) (ATP pyrophosphate-lyase 1) (Adenylate cyclase type I) (Adenylyl cyclase 1) (AC1) (Ca(2+)/calmodulin-activated adenylyl cyclase)
[CAMK1] Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (CaM kinase I alpha) (CaMKI-alpha)
[PDE1B PDE1B1 PDES1B] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (Cam-PDE 1B) (EC 3.1.4.17) (63 kDa Cam-PDE)
[CALM1 CALM CAM CAM1] Calmodulin-1
[Gap43 Basp2] Neuromodulin (Axonal membrane protein GAP-43) (Calmodulin-binding protein P-57) (Growth-associated protein 43)
[Pde1b Pde1b1] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (Cam-PDE 1B) (EC 3.1.4.17) (63 kDa Cam-PDE)
[Adcy1] Adenylate cyclase type 1 (EC 4.6.1.1) (ATP pyrophosphate-lyase 1) (Adenylate cyclase type I) (Adenylyl cyclase 1) (Ca(2+)/calmodulin-activated adenylyl cyclase)
[CNA1 CMP1 YLR433C L9753.6] Serine/threonine-protein phosphatase 2B catalytic subunit A1 (EC 3.1.3.16) (Calcineurin A1) (Calmodulin-binding protein 1)
[CAMK1G CLICK3 VWS1] Calcium/calmodulin-dependent protein kinase type 1G (EC 2.7.11.17) (CaM kinase I gamma) (CaM kinase IG) (CaM-KI gamma) (CaMKI gamma) (CaMKIG) (CaMK-like CREB kinase III) (CLICK III)
[Camk1] Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (CaM kinase I alpha) (CaMKI-alpha)

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[34572507] Subtype Differences in the Interaction of HIV-1 Matrix with Calmodulin: Implications for Biological Functions.
[34338988] CALM1 rs3179089 polymorphism might contribute to coronary artery disease susceptibility in Chinese male: a case-control study.
[33616872] Astrocyte Intracellular Caand TrkB Signaling in the Hippocampus Could Be Involved in the Beneficial Behavioral Effects of Antidepressant Treatment.
[33563308] Genetic markers of osteoarthritis: early diagnosis in susceptible Pakistani population.
[33546420] Tribbles Pseudokinase 2 (TRIB2) Regulates Expression of Binding Partners in Bovine Granulosa Cells.
[33280702] Effects of brain tissue section processing and storage time on gene expression.
[33233425] ACE2 Interaction Networks in COVID-19: A Physiological Framework for Prediction of Outcome in Patients with Cardiovascular Risk Factors.
[32625180] Molecular Analysis of S-morphology Aflatoxin Producers From the United States Reveals Previously Unknown Diversity and Two New Taxa.
[32522888] Elimination of long 3'-UTR mRNA isoform by CRISPR-Cas9 gene editing impairs dorsal root ganglion development and hippocampal neuron activation in mice.